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J. Biol. Chem., Vol. 266, Issue 19, 12201-12206, Jul, 1991
K Burdett, LK Larkins, AK Das and AK Hajra
Upon differential centrifugation of guinea pig intestine mucosal cells
homogenate, fatty acyl-CoA:NADPH oxidoreductase (long chain alcohol
forming) was found to be enriched in the light mitochondrial (L) fraction
(sedimenting between 66,000 x g min and 500,000 x g min) which contained
mainly mitochondria, lysosomes, and peroxisomes. Peroxisomes (marker
enzymes: catalase and dihydroxyacetone phosphate acyltransferase) present
in the L fraction were separated from other organelles in a Nycodenz
density gradient centrifugation employing a vertical rotor. By comparing
the distribution of acyl-CoA reductase with different marker enzymes in the
gradient, it was concluded that this reductase is primarily localized in
the microperoxisomes (microbodies). The topography of the membrane-bound
enzyme in the isolated organelles was studied by checking its lability
toward trypsin in the absence and presence of the detergent Triton X-100.
The results suggested that acyl-CoA reductase is localized on the outer
surface (cytosolic side) of microperoxisomal membrane.
Peroxisomal localization of acyl-coenzyme A reductase (long chain alcohol forming) in guinea pig intestine mucosal cells
Neuroscience Laboratory, University of Michigan, Ann Arbor 48104-1687.
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